Ontology type: schema:ScholarlyArticle
1996-11
AUTHORSPiotr Orlewski, Vassilios Tsikaris, Maria Sakarellos-Daitsiotis, Constantinos Sakarellos, Ketty P. Soteriadou, Michel Marraud, Manh Thong Cung
ABSTRACTThe IASRYDQL synthetic octapeptide (250–257) of the Leishmania major surface glycoprotein gp63 efficiently inhibits parasite attachment to the macrophage receptors in in vitro experiments, and the SRYD-containing tetrapeptide mimics antigenically and functionally the RGDS sequence of fibronectin. The conformational properties of the octapeptide were investigated in dimethylsulfoxide (DMSO) with the combined use of NMR data (vicinal coupling constants, nuclear Overhauser effects (NOEs) and temperature coefficient values), molecular modeling by energy minimization and molecular dynamics. The structure is characterized by the high occurrence, exceeding 95%, of the Arg-Asp side-chain-side-chain ionic interaction, which plays a key role in the backbone folding through a distorted type-I β-turn involving the Gln256-NH to Arg253-CO hydrogen bond. More... »
PAGES317-326
http://scigraph.springernature.com/pub.10.1007/bf00127666
DOIhttp://dx.doi.org/10.1007/bf00127666
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